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Dynamin−SNARE interactions control trans-SNARE formation in intracellular membrane fusion

Author

Listed:
  • Kannan Alpadi

    (Baylor College of Medicine)

  • Aditya Kulkarni

    (Baylor College of Medicine)

  • Sarita Namjoshi

    (Baylor College of Medicine)

  • Sankaranarayanan Srinivasan

    (Baylor College of Medicine)

  • Katherine H. Sippel

    (Baylor College of Medicine)

  • Kathryn Ayscough

    (University of Sheffield, Western Bank)

  • Martin Zieger

    (Université de Lausanne)

  • Andrea Schmidt

    (Université de Lausanne)

  • Andreas Mayer

    (Université de Lausanne)

  • Michael Evangelista

    (Baylor College of Medicine)

  • Florante A. Quiocho

    (Baylor College of Medicine)

  • Christopher Peters

    (Baylor College of Medicine)

Abstract

The fundamental processes of membrane fission and fusion determine size and copy numbers of intracellular organelles. Although SNARE proteins and tethering complexes mediate intracellular membrane fusion, fission requires the presence of dynamin or dynamin-related proteins. Here we study these reactions in native yeast vacuoles and find that the yeast dynamin homologue Vps1 is not only an essential part of the fission machinery, but also controls membrane fusion by generating an active Qa SNARE-tethering complex pool, which is essential for trans-SNARE formation. Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins.

Suggested Citation

  • Kannan Alpadi & Aditya Kulkarni & Sarita Namjoshi & Sankaranarayanan Srinivasan & Katherine H. Sippel & Kathryn Ayscough & Martin Zieger & Andrea Schmidt & Andreas Mayer & Michael Evangelista & Floran, 2013. "Dynamin−SNARE interactions control trans-SNARE formation in intracellular membrane fusion," Nature Communications, Nature, vol. 4(1), pages 1-8, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2724
    DOI: 10.1038/ncomms2724
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